Sequence of this protein is as follows: MASPSSFTYY CPPSSSPVWS EPLYSLRPEH ARERLQDDSV ETVTSIEQAK VEEKIQEVFS SYKFNHLVPR LVLQREKHFH YLKRGLRQLT DAYECLDASR PWLCYWILHS LELLDEPIPQ IVATDVCQFL ELCQSPEGGF GGGPGQYPHL APTYAAVNAL CIIGTEEAYD IINREKLLQY LYSLKQPDGS FLMHVGGEVD VRSAYCAASV ASLTNIITPD LFEGTAEWIA RCQNWEGGIG GVPGMEAHGG YTFCGLAALV ILKRERSLNL KSLLQWVTSR QMRFEGGFQG RCNKLVDGCY SFWQAGLLPL LHRALHAQGD PALSMSHWMF HQQALQEYIL MCCQCPAGGL LDKPGKSRDF YHTCYCLSGL SIAQHFGSGA MLHDVVLGVP ENALQPTHPV YNIGPDKVIQ ATTYFLQKPV PGFEELKDET SAEPATD
Eukaryotic cells contain 3 different types of prenyltransferases that attach either a farnesyl group (15 carbons) or a geranylgeranyl group (20 carbons) in thioether linkage to C-terminal cysteine residues in a variety of proteins. These posttranslational modifications provide a mechanism for membrane localization of proteins that lack a transmembrane domain. CAAX farnesyltransferase (FTase) attaches a farnesyl group from farnesyl pyrophosphate to cysteine residues at the fourth position from the C terminus of proteins that end in the CAAX box, where C is cysteine, A is usually but not always an aliphatic amino acid, and X is typically methionine or serine. This enzyme has the ability to farnesylate peptides as short as 4 residues in length that conform to the CAAX consensus sequence. The gene for the beta subunit of CAAX farnesyltransferase (FNTB) has been pinpointed to 14q23-q24 by Southern blot hybridization and PCR analyses of panels of human/Chinese hamster somatic cell hybrid lines and by fluorescence chromosomal in situ hybridization.
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Protein Aliases: CAAX farnesyltransferase subunit beta; EC 22.214.171.124; ft beta; FTase beta; FTase-beta; Protein farnesyltransferase subunit beta; Ras proteins prenyltransferase subunit beta
Gene Aliases: FNTB; FPTB
UniProt ID: (Human) P49356
Entrez Gene ID: (Human) 2342